Protein dynamics are an intrinsically important factor when considering a protein's biological function. Understanding these motions is often limited through the use of static structure determination methods, namely, X-ray crystallography and cryo-EM. Molecular simulations have allowed for the prediction of global and local motions of proteins from these static structures. Nevertheless, determining local dynamics at residue-specific resolution through direct measurement remains crucial....
[NMR paper] Dynamic membrane interactions of antibacterial and antifungal biomolecules, and amyloid peptides, revealed by solid-state NMR spectroscopy.
Dynamic membrane interactions of antibacterial and antifungal biomolecules, and amyloid peptides, revealed by solid-state NMR spectroscopy.
Related Articles Dynamic membrane interactions of antibacterial and antifungal biomolecules, and amyloid peptides, revealed by solid-state NMR spectroscopy.
Biochim Biophys Acta. 2017 Jun 06;:
Authors: Naito A, Matsumori N, Ramamoorthy A
Abstract
A variety of biomolecules acting on the cell membrane folds into a biologically active structure in the membrane environment. It is, therefore,...
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[NMR paper] Direct Determination of Site-specific Noncovalent Interaction Strengths of Proteins from NMR-derived Fast Side Chain Motional Parameters.
Direct Determination of Site-specific Noncovalent Interaction Strengths of Proteins from NMR-derived Fast Side Chain Motional Parameters.
Related Articles Direct Determination of Site-specific Noncovalent Interaction Strengths of Proteins from NMR-derived Fast Side Chain Motional Parameters.
J Phys Chem B. 2017 Apr 28;:
Authors: Tatikonda RR, Krishnan M
Abstract
A novel approach to accurately determine residue-specific noncovalent interaction strengths (?) of proteins from NMR-measured fast side chain motional parameters...
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[NMR paper] Studying Dynamics by Magic-Angle Spinning Solid-State NMR Spectroscopy: Principles and Applications to Biomolecules.
Studying Dynamics by Magic-Angle Spinning Solid-State NMR Spectroscopy: Principles and Applications to Biomolecules.
Studying Dynamics by Magic-Angle Spinning Solid-State NMR Spectroscopy: Principles and Applications to Biomolecules.
Prog Nucl Magn Reson Spectrosc. 2016 Aug;96:1-46
Authors: Schanda P, Ernst M
Abstract
Magic-angle spinning solid-state NMR spectroscopy is an important technique to study molecular structure, dynamics and interactions, and is rapidly gaining importance in biomolecular sciences. Here we provide an...
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Studying dynamics by magic-angle spinning solid-state NMR spectroscopy: Principles and applications to biomolecules
Studying dynamics by magic-angle spinning solid-state NMR spectroscopy: Principles and applications to biomolecules
Publication date: August 2016
Source:Progress in Nuclear Magnetic Resonance Spectroscopy, Volume 96</br>
Author(s): Paul Schanda, Matthias Ernst</br>
Magic-angle spinning solid-state NMR spectroscopy is an important technique to study molecular structure, dynamics and interactions, and is rapidly gaining importance in biomolecular sciences. Here we provide an overview of experimental approaches to study molecular dynamics by MAS solid-state NMR,...
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[NMR paper] Amplitudes and time scales of picosecond-to-microsecond motion in proteins studied by solid-state NMR: a critical evaluation of experimental approaches and application to crystalline ubiquitin.
Amplitudes and time scales of picosecond-to-microsecond motion in proteins studied by solid-state NMR: a critical evaluation of experimental approaches and application to crystalline ubiquitin.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles Amplitudes and time scales of picosecond-to-microsecond motion in proteins studied by solid-state NMR: a critical evaluation of experimental approaches and application to crystalline ubiquitin.
J Biomol NMR. 2013 Oct 9;
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[NMR paper] Determination of accurate 1H positions of an alanine tripeptide with anti-parallel and parallel ?-sheet structures by high resolution 1H solid state NMR and GIPAW chemical shift calculation.
Determination of accurate 1H positions of an alanine tripeptide with anti-parallel and parallel ?-sheet structures by high resolution 1H solid state NMR and GIPAW chemical shift calculation.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.rsc.org-images-entities-char_z_RSClogo.gif Related Articles Determination of accurate 1H positions of an alanine tripeptide with anti-parallel and parallel ?-sheet structures by high resolution 1H solid state NMR and GIPAW chemical shift calculation.
Chem Commun (Camb). 2012 Nov 25;48(91):11199-201
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Solid-state NMR spectroscopy on complex biomolecules.
Solid-state NMR spectroscopy on complex biomolecules.
Solid-state NMR spectroscopy on complex biomolecules.
Angew Chem Int Ed Engl. 2010 Nov 2;49(45):8346-57
Authors: Renault M, Cukkemane A, Baldus M
Biomolecular applications of NMR spectroscopy are often merely associated with soluble molecules or magnetic resonance imaging. However, since the late 1970s, solid-state NMR (ssNMR) spectroscopy has demonstrated its ability to provide atomic-level insight into complex biomolecular systems ranging from lipid bilayers to complex biomaterials. In the...
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[NMR paper] Practical methods for solid-state NMR distance measurements on large biomolecules: co
Practical methods for solid-state NMR distance measurements on large biomolecules: constant-time rotational resonance.
Related Articles Practical methods for solid-state NMR distance measurements on large biomolecules: constant-time rotational resonance.
J Magn Reson. 1999 Aug;139(2):371-6
Authors: Balazs YS, Thompson LK
Simple modifications of the rotational resonance experiment substantially reduce the total experimental time needed to measure weak homonuclear dipolar couplings, a critical factor for achieving routine internuclear distance...
Accurate Determination of Motional Amplitudes in Biomolecules by Solid-State NMR
Linear Mode
